Sequential disassembly of myofibrils induced by myristate acetate in cultured myotubes.

Lin, Zhenwu; Eshelman, J R; Forry-Schaudies, Suzanne; Duran, Sevin Teoman; Lessard, James L.; Holtzer, H.

doi:10.1083/jcb.105.3.1365

Cited by 53 publications

(54 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These two antibodies recognize epitopes at the Z-line and A-band, respectively, in striated skeletal and cardiac muscles (25,54). Monoclonal anti-sarcomeric myosin heavy chain (MHC) (F4G3), a gift from Dr. E Pepe (University of Pennsylvania, Philadelphia, PA), recognizes MHC from cardiac and skeletal muscle cells only (41,42). Affinity-purified polyclonal anti-desmoplakin is a gift from Dr. J. Nelson (Stanford University, Stanford, CA) and intensely stains desmosomes in MDCK cells (49).…”

Section: Antibodiesmentioning

confidence: 99%

The vinculin/sarcomeric-alpha-actinin/alpha-actin nexus in cultured cardiac myocytes

DiLullo

Schultheiss

et al. 1992

The Journal of Cell Biology

Self Cite

116

View full text Add to dashboard Cite

Abstract. Experiments are described supporting the proposition that the assembly of stress fibers in nonmuscle cells and the assembly of myofibrils in cardiac cells share conserved mechanisms. Double staining with a battery of labeled antibodies against membraneassociated proteins, myofibrillar proteins, and stress fiber proteins reveals the following: (a) dissociated, cultured cardiac myocytes reconstitute intercalated discs consisting of adherens junctions (AJs) and desmosomes at sites of cell-cell contact and sub-sarcolemmal adhesion plaques (SAPs) at sites of cellsubstrate contact; (b) each AJ or SAP associates proximally with a striated myofibril, and conversely every striated myofibril is capped at either end by an AJ or a SAP; (C) the invariant association between a given myofibril and its SAP is especially prominent at the earliest stages of myofibrillogenesis; nascent myofibrils are capped by oppositely oriented SAPs; (d) the insertion of nascent myofibrils into AJs or into SAPs invariably involves vinculin, a-actin, and sarcomeric ot-actinin (s-ot-actinin); (e) AJs are positive for A-CAM but negative for talin and integrin; SAPs lack A-CAM but are positive for talin and integrin; (f) in cardiac cells all ot-actinin-containing structures invariably are positive for the sarcomeric isoform, o~-actin and related sarcomeric proteins; they lack non-sot-actinin, -y-actin, and caldesmon; (g) in fibroblasts all ot-actinin-containing structures are positive for the non-sarcomeric isoform, -y-actin, and related nonsarcomeric proteins, including caldesmon; and (h) myocytes differ from all other types of adherent cultured cells in that they do not assemble authentic stress fibers; instead they assemble stress fiber-like structures of linearly aligned I-Z-I-like complexes consisting exclusively of sarcomeric proteins. CONSIDERABLE information has accumulated regarding the molecular composition and possible functions of the submembranous complexes into which stress fibers insert (4,5,11,26,34,46). In cell-cell junctions of the adherens type the distal tips of the microfilament bundles insert into submembranous F-actin/o~-actinin/vinculin complexes that often involve additional membrane-associated molecules such as A-CAM (31, 60), radixin (58) etc. A somewhat different class of submembranous complexes characterizes the termini of stress fibers where they insert into the cell-substrate junctions of spread, nontranslocating cultured ceils. These F-actin/ot-actinin/vinculin complexes, known as adhesion plaques (APs),t are also positive for talin (11), paxillin (59), integrin (17), and other proteins. APs are also sites for a Ca2 § protease (5) and a1. Abbreviations used in this paper: AJ, adherens junction; AP, adhesion plaque; MHC, myosin heavy chain; s, sarcomeric; SAP, subsarcolemmal adhesion plaque.protein kinase C (35) suggesting they may be involved in transmembrane signaling. In both the adherens junction (AJs) and the APs, ct-actinin appears to play a bifunctional role. Distally, facing the inner surface of the c...

show abstract

Section: Antibodiesmentioning

confidence: 99%

The vinculin/sarcomeric-alpha-actinin/alpha-actin nexus in cultured cardiac myocytes

DiLullo

Schultheiss

et al. 1992

The Journal of Cell Biology

Self Cite

116

View full text Add to dashboard Cite

show abstract

“…Treated myotubes were stained with fluorescein-labeled antibodies to a-actinin and with rhodamine-labeled phalloidin, which binds to all filamentous actin. Lin et al (43) …”

Section: Resultsmentioning

confidence: 99%

“…By studying the MATERIALS AND METHODS Culture. Chick skeletal muscle cultures were obtained as previously described (43). Cytosine arabinonucleoside (Ara-C; i0' M) was introduced 2 to 3 days after initial plating and was used throughout the experiments to remove replicating fibroblastic cells.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Phorbol esters selectively and reversibly inhibit a subset of myofibrillar genes responsible for the ongoing differentiation program of chick skeletal myotubes.

Choi¹,

Holtzer²,

Chacko³

et al. 1991

Mol. Cell. Biol.

Self Cite

View full text Add to dashboard Cite

Phorbol esters selectively and reversibly disassemble the contractile apparatus of cultured skeletal muscle as well as inhibit the synthesis of many contractile proteins without inhibiting that of housekeeping proteins. We now demonstrate that phorbol esters reversibly decrease the mRNA levels of at least six myofibrillar genes: myosin heavy chain, myosin light chain 1/3, myosin light chain 2, cardiac and skeletal a-actin, and skeletal troponin T. The steady-state message levels decrease 50-to 100-fold after 48 h of exposure to phorbol esters. These decreases can be attributed at least in part to decreases in transcription rates. For at least two genes, cardiac and skeletal a-actin, some of the decreases are the result of increased mRNA turnover. In contrast, the cardiac troponin T steady-state message level does not change, and its transcription rate decreases only transiently upon exposure to phorbol esters. Phorbol esters do not decrease the expression of the housekeeping genes, a-tubulin, 0-actin, and -y-actin. Phorbol esters do not decrease the steady-state message levels of MyoDl, a gene known to be important in the activation of many skeletal muscle-specific genes. Cycloheximide blocks the phorbol ester-induced decreases in transcription, message stability, and the resulting steady-state message level but does not block the tetradecanoyl phorbol acetate-induced rapid disassembly of the I-Z-I complexes. These results suggests a common mechanism for the regulation of many myofibrillar genes independent of MyoDl mRNA levels, independent of housekeeping genes, but dependent on protein synthesis.

show abstract

“…Similarly, latrunculin-A, an inhibitor of actin polymerization, prevented the formation of premyofibrils but did not perturb mature myofibrils . Mature myofibrils are however disassembled by the overexpression of an N-terminal fragment of titin or by phorbol ester treatment [Lin et al, 1987;Turnacioglu et al, 1997]. However, these treatments have not been shown to perturb the MT array whereas myoseverin displays an apparent dual action in inhibiting both myofibrils and polymerized tubulin.…”

Section: Myoseverin Is a Dual-action Disruptor Of The Cytoskeletonmentioning

confidence: 99%

Myoseverin disrupts sarcomeric organization in myocytes: An effect independent of microtubule assembly inhibition

Gebski

Grounds

et al. 2007

Cell Motil. Cytoskeleton

View full text Add to dashboard Cite

Although disruption of the microtubule (MT) array inhibits myogenesis in myocytes, the relationship between the assembly of microtubules (MT) and the organization of the contractile filaments is not clearly defined. We now report that the assembly of mature myofibrils in hypertrophic cardiac myocytes is disrupted by myoseverin, a compound previously shown to perturb the MT array in skeletal muscle cells. Myoseverin treated cardiac myocytes showed disruptions of the striated Z-bands containing a-actinin and desmin and the localization of tropomyosin, titin and myosin on mature sarcomeric filaments. In contrast, MT depolymerization by nocodazole did not perturb sarcomeric filaments. Similarly, expression of constitutively active stathmin as a non-chemical molecular method of MT depolymerization did not prevent sarcomere assembly. The extent of MT destabilization by myoseverin and nocodazole were comparable. Thus, the effect of myoseverin on sarcomere assembly was independent of its capacity for MT inhibition. Furthermore, we found that upon removal of myoseverin, sarcomeres reformed in the absence of an intact MT network. Sarcomere formation in cardiac myocytes therefore, does not appear to require an intact MT network and thus we conclude that a functional MT array appears to be dispensable for myofibrillogenesis. Cell Motil. Cytoskeleton 65: 40-58, 2008. '

show abstract

Sequential disassembly of myofibrils induced by myristate acetate in cultured myotubes.

Cited by 53 publications

References 50 publications

The vinculin/sarcomeric-alpha-actinin/alpha-actin nexus in cultured cardiac myocytes

The vinculin/sarcomeric-alpha-actinin/alpha-actin nexus in cultured cardiac myocytes

Phorbol esters selectively and reversibly inhibit a subset of myofibrillar genes responsible for the ongoing differentiation program of chick skeletal myotubes.

Myoseverin disrupts sarcomeric organization in myocytes: An effect independent of microtubule assembly inhibition

Contact Info

Product

Resources

About